title: NMR localization of the O-mycoloylation on PorH, a channel forming peptide from Corynebacterium glutamicum.
abstract: PorH and PorA are two small peptides that, in complex, form a voltage-dependent ion channel in the outer membrane of Corynebacterium glutamicum. Specific post-translational modifications on PorA and PorH are required for the formation of a functional ion channel. The assignment of PorH proton NMR chemical shifts in DMSO, allowed identifying unambiguously the exact position of the PorH O-mycoloylation on Ser 56 side chain. This was further confirmed by site directed mutagenesis and mass spectrometry. Together with the previously published localization of PorA mycoloylation, this provides the complete primary structure characterization of this outer membrane porin.
authors.affiliation: Institute of Pharmacology and Structural Biology, Université de Toulouse, UPS, 205 route de Narbonne, 31077 Toulouse, France; IPBS, UMR 5089, CNRS, 205 route de Narbonne, BP 64182, 31077 Toulouse, France.
authors.forename: Parthasarathi
authors.initials: P
authors.lastname: Rath
authors.forename: Olivier
authors.initials: O
authors.lastname: Saurel
authors.forename: Maryelle
authors.initials: M
authors.lastname: Tropis
authors.forename: Mamadou
authors.initials: M
authors.lastname: Daffé
authors.forename: Pascal
authors.initials: P
authors.lastname: Demange
authors.forename: Alain
authors.initials: A
authors.lastname: Milon
mesh_terms: D000595:Amino Acid Sequence; D048230:Corynebacterium glutamicum; D054878:Lipoylation; D008969:Molecular Sequence Data; D009171:Mycolic Acids / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D018272:Porins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012694:Serine / Q000378:metabolism*
chemical_list: D009171:Mycolic Acids; D018272:Porins; D012694:Serine
keywords: HSQC-NOESY; HSQC-TOCSY; Ion channel; MALDI-TOF; Mycolic acid; Post translational modification